Evidence map›Paper›PMID 8781383›Full record

ArticleEnvironmental health perspectives1996

Involvement of cytochrome P450, glutathione S-transferase, and epoxide hydrolase in the metabolism of aflatoxin B1 and relevance to risk of human liver cancer.

F P Guengerich, W W Johnson, Y F Ueng, H Yamazaki, T Shimada

Open access · diamondAbstract read
In one paragraph

Article in Environmental health perspectives, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.2field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Phenoconversion andHepatology forum · 2025
    Review
  8. Article
  9. Mass Spectrometry-Based Method to Measure Aflatoxin BChemical research in toxicology · 2024
    Article
  10. Comparative metabolism of aflatoxin BArchives of toxicology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. QuEChERS LC-MS/MS Screening Method for Mycotoxin Detection in Cereal Products and Spices.International journal of environmental research and public health · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. Anti-mutagenic and Anti-oxidant Potencies ofIranian journal of pharmaceutical research : IJPR · 2018
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

F P GuengerichDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA. guengerich@toxicology.mc.vanderbilt.edu
W W Johnson
Y F Ueng
H Yamazaki
T Shimada
Vanderbilt University · US

Funding

Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
ENZYMIC ACTIVATION OF CHEMICAL CARCINOGENSR35CA044353 · NCI · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1987 to 2000
$974k
NCI NIH HHS CA44353NIEHS NIH HHS ES00267
6 · The paper itself

Abstract

In recent years there has been considerable interest in the effect of variations in activities of xenobiotic-metabolizing enzymes on cancer incidence. This interest has accelerated with the development of methods for analyzing genetic polymorphisms. However, progress in epidemiology has been slow and the contributions of polymorphisms to risks from individual chemicals and mixtures are often controversial. A series of studies is presented to show the complexities encountered with a single chemical, aflatoxin B1 (AFB1). AFB1 is oxidized by human cytochrome P450 enzymes to several products. Only one of these, the 8,9-exo-epoxide, appears to be mutagenic and the others are detoxication products. P450 3A4, which can both activate and detoxicate AFB1, is found in the liver and the small intestine. In the small intestine, the first contact after oral exposure, epoxidation would not lead to liver cancer. The (nonenzymatic) half-life of the epoxide has been determined to be approximately 1 sec at 23 degrees C and neutral pH. Although the half-life is short, AFB1-8,9-exo-epoxide does react with DNA and glutathione S-transferase. Levels of these conjugates have been measured and combined with the rate of hydrolysis in a kinetic model to predict constants for binding of the epoxide with DNA and glutathione S-transferase. A role for epoxide hydrolase in alteration of AFB1 hepatocarcinogenesis has been proposed, although experimental evidence is lacking. Some inhibition of microsome-generated genotoxicity was observed with rat epoxide hydrolase; further information on the extent of contribution of this enzyme to AFB1 metabolism is not yet available.

Indexed as

Aflatoxin B1AnimalsCarcinogensCytochrome P-450 Enzyme SystemDNA AdductsEpoxide HydrolasesEscherichia coliGlutathione TransferaseHumansHydrolysisLiver NeoplasmsOxidation-ReductionRatsRecombinant ProteinsAflatoxin B1CarcinogensCytochrome P-450 Enzyme SystemDNA AdductsEpoxide HydrolasesGlutathione TransferaseRecombinant Proteins

Identifiers

PMID8781383
PMCPMC1469621
OpenAlexW2072634355

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.